PVPS_TALVE
ID PVPS_TALVE Reviewed; 778 AA.
AC A0A2Z6AQX6;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Preasperterpenoid A synthase PvPS {ECO:0000303|PubMed:28671289};
DE AltName: Full=Bifunctional sesterterpene synthase PvPS {ECO:0000303|PubMed:28671289};
DE Short=PS {ECO:0000303|PubMed:28671289};
DE Includes:
DE RecName: Full=Preasperterpenoid A cyclase {ECO:0000303|PubMed:28671289};
DE EC=4.2.3.- {ECO:0000269|PubMed:28671289, ECO:0000269|PubMed:32378547};
DE Includes:
DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:28671289};
DE Short=GGDP synthase {ECO:0000303|PubMed:28671289};
DE Short=GGS {ECO:0000303|PubMed:28671289};
DE EC=2.5.1.29 {ECO:0000269|PubMed:28671289};
DE Includes:
DE RecName: Full=Geranylfarnesyl diphosphate synthase {ECO:0000303|PubMed:28671289};
DE Short=GFDP synthase {ECO:0000303|PubMed:28671289};
DE EC=2.5.1.81 {ECO:0000269|PubMed:28671289};
GN Name=PvPS {ECO:0000303|PubMed:28671289};
OS Talaromyces verruculosus (Penicillium verruculosum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=198730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=TPU1311;
RX PubMed=28671289; DOI=10.1002/chem.201702766;
RA Mitsuhashi T., Rinkel J., Okada M., Abe I., Dickschat J.S.;
RT "Mechanistic Characterization of Two Chimeric Sesterterpene Synthases from
RT Penicillium.";
RL Chemistry 23:10053-10057(2017).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32378547; DOI=10.1248/cpb.c20-00037;
RA Sato H., Yamazaki M., Uchiyama M.;
RT "DFT study on the biosynthesis of preasperterpenoid A: role of secondary
RT carbocations in the carbocation cascade.";
RL Chem. Pharm. Bull. 68:487-490(2020).
CC -!- FUNCTION: Bifunctional sesterterpene synthase that possesses both
CC prenyl transferase and terpene cyclase activity, converting isopentenyl
CC diphosphate and dimethylallyl diphosphate into geranylfarnesyl
CC diphosphate (GFPP) and further converting GFPP into preasperterpenoid
CC A. {ECO:0000269|PubMed:28671289, ECO:0000269|PubMed:32378547}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate =
CC (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate;
CC Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
CC Evidence={ECO:0000269|PubMed:28671289};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC Evidence={ECO:0000269|PubMed:28671289};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl
CC diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate +
CC diphosphate; Xref=Rhea:RHEA:25694, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57907, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769;
CC EC=2.5.1.81; Evidence={ECO:0000269|PubMed:28671289};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25695;
CC Evidence={ECO:0000269|PubMed:28671289};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E,14E)-geranylfarnesyl diphosphate = diphosphate +
CC preasperterpenoid A; Xref=Rhea:RHEA:66832, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57907, ChEBI:CHEBI:167511;
CC Evidence={ECO:0000269|PubMed:28671289, ECO:0000269|PubMed:32378547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66833;
CC Evidence={ECO:0000269|PubMed:28671289};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WEV7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:28671289}.
CC -!- SUBUNIT: Hexamer. {ECO:0000250|UniProtKB:A2PZA5}.
CC -!- DOMAIN: The conserved DDXXD motifs as well as the NSE/DTE motif are
CC important for the catalytic activity, presumably through binding to
CC Mg(2+). {ECO:0000250|UniProtKB:P9WEV6}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the terpene synthase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the FPP/GGPP synthase
CC family. {ECO:0000305}.
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DR EMBL; LC228602; BBD05405.1; -; Genomic_DNA.
DR SMR; A0A2Z6AQX6; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 2.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 2.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW Isoprene biosynthesis; Lyase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Repeat; Transferase.
FT CHAIN 1..778
FT /note="Preasperterpenoid A synthase PvPS"
FT /id="PRO_0000453791"
FT REGION 1..414
FT /note="Terpene cyclase"
FT /evidence="ECO:0000305|PubMed:28671289"
FT REGION 415..778
FT /note="Prenyltransferase"
FT /evidence="ECO:0000305|PubMed:28671289"
FT REGION 416..454
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:M2V8C1"
FT MOTIF 176..180
FT /note="DDXXD 1"
FT /evidence="ECO:0000250|UniProtKB:A1C8C3"
FT MOTIF 310..318
FT /note="NSE/DTE"
FT /evidence="ECO:0000250|UniProtKB:A1C8C3"
FT MOTIF 538..542
FT /note="DDXXD 2"
FT /evidence="ECO:0000250|UniProtKB:A1C8C3"
FT COMPBIAS 414..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 266..269
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 314..318
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 406..407
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 499
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 502
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 531
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 547
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 548
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 625
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 626
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 662
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 669
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 679
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 689
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 778 AA; 87884 MW; 0485E61AB9C5DC71 CRC64;
MAATKKSTAT AAHQIIPSQP TSMSADKFLF SCLQVFVLFF EWARSFLLST QSRLSAVPAE
NARLEPSKPI SEEEESVIEK PASSITPRYS NLVDPSTYND LGLCSALPLR VHKFAHLADK
GALRAQEDWK RLVGPIRNFT GCLSPRFNGI AVAVPECIPE RLEIVTYANE FAFLHDDILD
NVGKEEGDHE NNEMAAGFGS VLNPADNVKM SASGKSQMQA KLILELLAIN EPQAMVLLKC
WEGLVKGESG SQHFNFQRLD EYLPHRVINL GQTFWFGIIT FAMGLTISPD EAEKANNITD
PAYATLALAN DYFSWEKEYI EFKQNPTSDD MANAIWIIMK EHSVDLEEAK KICQDKIRES
CEEYVRRHRQ FEREATGKVS TDLLRYLAAL EFSISGNVVW SQYTHRYNFH KPAAKENEDT
DDEGAKSDDS KTTLNDSTDS TVVDVKTPAT SGLLSSANDV LMSRTAKSLV GPILDVQLPE
LPDKVVLSPS QYVKSLPSKK VRHHAIDALN IWFNVPEAEL EVIKEAIDLL HNSSLMLDDI
EDDSPLRRGF PSTHVVYGIS QTINSANYLY VMALEMTQRL NSPACLNVFI DELKRLHIGQ
SLDLYWTANV QCPSLEEYLK MVDYKTGGLF QMVAKLMALK SPMAGRVPDL SNMTTLFGRY
FQIRDDYQNL MSEEYTNQKG WCEDLDEGKF SLPLIHSLTT KPNVRLQAML HQRLINGKMT
FEMKKLALDH LAETKSLEYT KEMLGYMYTQ LQKEVDFLER QTGSENFLLR LLLKRLQV
